UBE2D3, human recombinant

Catalog number: SBB-CE0019, 100 μg

UBE2D3 is an E2 conjugating enzyme which catalyzes the E3 mediated ubiquitination of a target substrate. It is known to interact in conjunction with E3 ligase MDM2 to ubiquitinate p53. This protein is recombinantly expressed in E.coli.[1][2]

In stock
SKU
0019
$179.00

Description

UBE2D3 is an E2 ubiquitin conjugating enzyme. An E1 activating enzyme is required to attach ubiquitin to UBE2D3 via an active site cysteine. The mechanism of ubiquitin transfer involves the breaking of a E1-Ub thioester linkage, followed by a reformation of a UBE2D3-Ub thioester. UBE2D3 is capable of associating with numerous known E3 ligases including MDM2, which target proteins such as p53 for proteasomal degradation through polyubiquitination. This recombinant UBE2D3 is expressed in E.coli. Working concentrations of this enzyme range from 1 to 5µM.

For Research Use Only, Not For Use In Humans.

Specifications

Product Overview
Quantity: 100 μg
Molecular Weight: 17 kDa
Purity: >95% by SDS-PAGE
Substrate Properties: Working concentrations of this enzyme range from 1 to 5µM.
Storage Buffer: 50 mM HEPES pH 8.0, 200 mM NaCl, 10% Glycerol, 1 mM TCEP
Storage Store at −80°C after product arrival. Avoid multiple freeze / thaws. It is recommended to make multiple aliquots after the first thaw.

Figures & Data

UBE2D3, human recombinant

Figure 1. UBE2D3, SDS-PAGE From left to right, increasing amounts of UBE2D3 loaded onto a 4-20% SDS-PAGE gel, stained with coomassie brilliant blue. UBE2D3 is > 95% pure.

E2 Thioester Activity

Figure 2. Thioester Activity Assay. UBE2D3 forms a thioester with UB in an ATP dependent manner, and the bond can be reduced with addition of access DTT. The UBE2D3 is active.

Citations & References

1) Geisler, Sven, et al. “The ubiquitin-conjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy.” J Cell Sci 127.15 (2014): 3280-3293.

2) Smit, Judith J., et al. “The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension.” The EMBO journal 31.19 (2012): 3833-3844.